Is the molten globule a third phase of proteins?
The equilibrium properties of proteins are studied by Monte Carlo simulation of two simplified models of protein-like heteropolymers. These models emphasize the polymeric entropy of the fluctuating polypeptide chain. Our calculations suggest a generic phase diagram that contains a thermodynamically distinct "molten globule" state in addition to a rigid native state and a nontrivial unfolded state. The roles of side-chain packing and loop entropy are discussed.
Pande
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VS
Department of Physics, University of California at Berkeley, Berkeley, CA 94720, USA.
Rokhsar
D S
DS
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D019277:Entropy; D006860:Hydrogen Bonding; D008954:Models, Biological; D009010:Monte Carlo Method; D011108:Polymers; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013205:Staphylococcal Protein A; D013696:Temperature; D013816:Thermodynamics
D011108:Polymers; D011506:Proteins; D013205:Staphylococcal Protein A